ID   OMCBC_CHLTH             Reviewed;         547 AA.
AC   P26758;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Large cysteine-rich periplasmic protein OmcB, serovar C;
DE            Short=Large-CRP;
DE   AltName: Full=60 kDa CRP;
DE   AltName: Full=60 kDa outer membrane protein;
DE   AltName: Full=Cysteine-rich outer membrane protein;
DE   Flags: Precursor;
GN   Name=omcB; Synonyms=omp2, omp2B;
OS   Chlamydia trachomatis.
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C/TW-3;
RX   PubMed=1997423; DOI=10.1128/iai.59.3.1196-1201.1991;
RA   de la Maza L.M., Fiedler T.J., Carlson E.J., Markoff B.A., Peterson E.M.;
RT   "Sequence diversity of the 60-kilodalton protein and of a putative 15-
RT   kilodalton protein between the trachoma and lymphogranuloma venereum
RT   biovars of Chlamydia trachomatis.";
RL   Infect. Immun. 59:1196-1201(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C/TW-3;
RA   Zhang Y.-X., Caldwell H.D.;
RT   "The nucleotide sequences of 10 and 60 kDa cysteine-rich outer membrane
RT   protein genes of Chlamydia trachomatis serovar F.";
RL   Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: In elementary bodies (EBs, the infectious stage, which is
CC       able to survive outside the host cell) provides the structural
CC       integrity of the outer envelope through disulfide cross-links with the
CC       small cysteine-rich protein and the major outer membrane porin. It has
CC       been described in publications as the Sarkosyl-insoluble COMC
CC       (Chlamydia outer membrane complex), and serves as the functional
CC       equivalent of peptidoglycan (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Part of a disulfide cross-linked outer membrane complex (COMC)
CC       composed of the major outer membrane porin (MOMP), the small cysteine-
CC       rich protein (OmcA) and the large cysteine-rich periplasmic protein
CC       (OmcB). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: It is present but the disulfide bonds are reduced
CC       in the intracellular reticulate bodies (RBs).
CC   -!- CAUTION: Was thought to be an outer membrane protein as it is part of a
CC       disulfide cross-linked complex that is insoluble in the detergent
CC       Sarkosyl; however based on experiments in C.psittaci it is likely to be
CC       periplasmic. {ECO:0000305}.
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DR   EMBL; X54388; CAA38257.1; -; Genomic_DNA.
DR   EMBL; M85197; AAA23159.1; -; Genomic_DNA.
DR   PIR; D71515; D71515.
DR   RefSeq; WP_015505969.1; NZ_CP018052.1.
DR   AlphaFoldDB; P26758; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR003506; Chlam_OMP6.
DR   InterPro; IPR001434; DUF11.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF03504; Chlam_OMP6; 1.
DR   Pfam; PF01345; DUF11; 3.
DR   PRINTS; PR01336; CHLAMIDIAOM6.
DR   TIGRFAMs; TIGR01451; B_ant_repeat; 2.
PE   2: Evidence at transcript level;
KW   Cell shape; Disulfide bond; Periplasm; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..40
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000020168"
FT   CHAIN           41..547
FT                   /note="Large cysteine-rich periplasmic protein OmcB,
FT                   serovar C"
FT                   /id="PRO_0000020169"
FT   REGION          45..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..77
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   547 AA;  58680 MW;  817BA5DC7FEA65D4 CRC64;
     MNKLIRRAVT IFAVTSVASL FASGVLETSM AESLSTNVIS LADTKAKDNT SHKSKKARKN
     HSKETPVDRK EVAPVHESKA TGPKQDSCFG RMYTVKVNDD RNVEITQAVP EYATVGSPYP
     IEITATGKRD CVDVIITQQL PCEAEFVRSD PATTPTADGK LVWKIDRLGQ GEKSKITVWV
     KPLKEGCCFT AATVCACPEI RSVTKCGQPA ICVKQEGPEN ACLRCPVVYK INVVNQGTAT
     ARNVVVENPV PDGYAHSSGQ RVLTFTLGDM QPGEHRTITV EFCPLKRGRA TNIATVSYCG
     GHKNTASVTT VINEPCVQVS IAGADWSYVC KPVEYVISVS NPGDLVLRDV VVEDTLSPGV
     TVLEAAGAQI SCNKVVWTVK ELNPGESLQY KVLVRAQTPG QFTNNVVVKS CSDCGTCTSC
     AEATTYWKGV AATHMCVVDT CDPVCVGENT VYRICVTNRG SAEDTNVSLM LKFSKELQPV
     SFSGPTKGTI TGNTVVFDSL PRLGSKETVE FSVTLKAVSA GDARGEAILS SDTLTVPVSD
     TENTHIY